Illustration by H.D. Vishwarao, K.A. Kasischke, M.A. Williams and W.W. Webb
The image above is from the cover of the July 1 issue of the Journal of Biological Chemistry and relates to a "paper of the week" article titled "Conformational dependence of intracellular NADH on metabolic state revealed by associated fluorescence anisotrophy," by H.D. Vishwasrao, A.A. Heikal, K.A. Kasischke and W.W. Webb. Caption: "Metabolic dynamics in the brain are imaged using the fluorescence of endogenous reduced beta-nicotinamide adenine dinucleotide (NADH). Fluorescence measurements, however, are complicated by the dependence of the quantum efficiency of NADH on its free/bound state. Time-resolved fluorescence anisotropy discriminates free/bound NADH and shows a preferential increase in free NADH during the normoxic (blue curve) to hypoxic (red curve) metabolic transition."
By discovering a crucial piece of submicroscopic information about how the brain converts fuel into energy for neurons, Cornell University biophysicists have gleaned new insights into brain cell metabolism that will allow neurologists to better interpret data from such diagnostic tests as positron emission tomography (PET) scans and a specialized magnetic resonance imaging (MRI) test.
The discovery uncovers a key piece of information that’s been missing for years about cell metabolism -- how the compound beta-nicotinamide adenine dinucleotide (NADH) interacts in the mitochondria. The researchers discovered that some molecules of NADH are bound to other molecules in the mitochondria, while some are free in two different conformations. Whether NADH is bound or free affects how much it fluoresces in diagnostic tests -- and not knowing this has led scientists in the past to misjudge the amount of activity in neural cells.
The findings, published as a paper of the week in the July 1 issue of the Journal of Biological Chemistry (Vol. 280), are based on research in the biophysics lab directed by Watt W. Webb, the S.B. Eckert Professor in Engineering at Cornell. The journal’s cover illustration was designed by Webb with images from his biophysics lab by Karl Kasischke, Harshad Vishwasrao and Dan Dombeck.
Blaine P. Friedlander Jr. | EurekAlert!
Study tracks inner workings of the brain with new biosensor
16.08.2018 | Rheinische Friedrich-Wilhelms-Universität Bonn
Foods of the future
15.08.2018 | Georg-August-Universität Göttingen
New design tool automatically creates nanostructure 3D-print templates for user-given colors
Scientists present work at prestigious SIGGRAPH conference
Most of the objects we see are colored by pigments, but using pigments has disadvantages: such colors can fade, industrial pigments are often toxic, and...
Scientists at the University of California, Los Angeles present new research on a curious cosmic phenomenon known as "whistlers" -- very low frequency packets...
Scientists develop first tool to use machine learning methods to compute flow around interactively designable 3D objects. Tool will be presented at this year’s prestigious SIGGRAPH conference.
When engineers or designers want to test the aerodynamic properties of the newly designed shape of a car, airplane, or other object, they would normally model...
Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.
Global demand for electric vehicles is forecast to rise sharply: by 2025, the number of new vehicle registrations is expected to reach 25 million per year....
Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...
17.08.2018 | Event News
08.08.2018 | Event News
27.07.2018 | Event News
17.08.2018 | Physics and Astronomy
17.08.2018 | Information Technology
17.08.2018 | Life Sciences